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Structure paper

TitleMechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures.
Journal, issue, pagesJ. Mol. Biol., Vol. 309, Page 239-254, Year 2001
Publish dateDec 8, 2000 (structure data deposition date)
AuthorsKnofel, T. / Strater, N.
External linksJ. Mol. Biol. / PubMed:11491293
MethodsX-ray diffraction
Resolution1.7 - 2.1 Å
Structure data

PDB-1ho5:
5'-NUCLEOTIDASE (E. COLI) IN COMPLEX WITH ADENOSINE AND PHOSPHATE
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1hp1:
5'-NUCLEOTIDASE (OPEN FORM) COMPLEX WITH ATP
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-1hpu:
5'-NUCLEOTIDASE (CLOSED FORM), COMPLEX WITH AMPCP
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-ADN:
ADENOSINE

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-CO3:
CARBONATE ION

ChemComp-SO4:
SULFATE ION

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-A12:
PHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / metalloprotein / domain movement / metallophosphatase / dinuclear / metalloenzyme / domain rotation

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